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The major function of RIP1 (show UQCRFS1 Proteins) kinase activity in TNF (show TNF Proteins)-induced necroptosis is to autophosphorylate serine 161. This specific phosphorylation then enables RIP1 (show UQCRFS1 Proteins) to recruit RIP3 (show RIPK3 Proteins) and form a functional necrosome, a central controller of necroptosis.
In lesional psoriatic epidermis, RIPK1-expression was decreased compared with that in normal epidermis. RIPK1-knockdown enhanced TRAIL-mediated expression of psoriasis-relating cytokines in normal human epidermal keratinocytes.
RIPK1 plays a critical role in the human immune system.
Elevated A20 (show TNFAIP3 Proteins) promotes TNF (show TNF Proteins)-induced and RIPK1-dependent intestinal epithelial cell death
RIPK1-DD has a role in mediating RIPK1 dimerization and activation of its kinase activity during necroptosis and RIPK1-dependent apoptosis
We further identified this underlying mechanism also involved a PPARgamma (show PPARG Proteins)-induced ANXA1 (show ANXA1 Proteins)-dependent autoubiquitination of cIAP1 (show BIRC2 Proteins), the direct E3 ligase of RIP1 (show UQCRFS1 Proteins), shifting cIAP1 (show BIRC2 Proteins) toward proteosomal degradation..our study provides first insight for the suitability of using drug-induced expression of ANXA1 (show ANXA1 Proteins) as a new player in RIP1 (show UQCRFS1 Proteins)-induced death machinery in triple-negative breast cancer
data suggest that artesunate could induce RIP1-dependent cell death in human renal carcinoma.
RIP1 (show UQCRFS1 Proteins) has a role in CD40 (show CD40 Proteins)-mediated activation of caspase-8 (show CASP8 Proteins), which in turn leads to induction of apoptosis
High RIPK1 expression is associated with Alzheimer's disease.
These data represent the first report of decreased RIPK1 expression in neutrophils of Systemic Lupus Erythematosus patients and imply that RIPK1 may be involved in neutrophil death and neutrophil extracellular traps formation.
Aldehyde dehydrogenase 2 deficiency negates chronic low-to-moderate alcohol consumption-induced cardioprotecion possibly via ROS-dependent apoptosis and RIP1/RIP3/MLKL-mediated necroptosis.
The major function of RIP1 (show RALBP1 Proteins) kinase activity in TNF (show TNF Proteins)-induced necroptosis is to autophosphorylate serine 161. This specific phosphorylation then enables RIP1 (show RALBP1 Proteins) to recruit RIP3 and form a functional necrosome, a central controller of necroptosis.
two different modes of necroptosis induction by TNFalpha (show TNF Proteins) exist which are differentially regulated by iuRIPK1 formation. Overall, this work reveals a distinct mechanism of RIPK1 activation that mediates the signaling mechanism of RDA as well as a type of necroptosis.
We show that inflammation and autoimmunity are prevented upon expression of kinase inactive RIPK1 or deletion of RIPK3 (show RIPK3 Proteins) or MLKL. We provide evidence that the inflammation is not driven by microbial ligands, but depends on the release of danger-associated molecular patterns and MyD88 (show MYD88 Proteins)-dependent signaling.
RIPK1 kinase activity mediates TWEAK (show TNFSF12 Proteins)-induced apoptosis.
The authors report here that male reproductive organs of both Ripk3 (show RIPK3 Proteins)- and Mlkl-knockout mice retain 'youthful' morphology and function into advanced age, while those of age-matched wild-type mice deteriorate. Feeding of wild-type mice with an RIPK1 inhibitor prior to the normal onset of age-related changes in their reproductive organs blocked the appearance of signs of aging.
Pull down experiments with biotinylated Sorafenib show that it binds independently RIPK1, RIPK3 (show RIPK3 Proteins) and MLKL. Moreover, it inhibits RIPK1 and RIPK3 (show RIPK3 Proteins) kinase activity. In vivo Sorafenib protects against TNF (show TNF Proteins)-induced systemic inflammatory response syndrome (SIRS) and renal ischemia-reperfusion injury (IRI).
Interaction of xFADD and xRIP1 induced synergistic activation of JNK (show MAPK8 Proteins) and NF-kappaB (show NFKB1 Proteins).
Serine-threonine kinase which transduces inflammatory and cell-death signals (necroptosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necroptosis-inducing complex.
, cell death protein RIP
, receptor interacting protein
, receptor-interacting protein 1
, receptor-interacting serine/threonine-protein kinase 1
, serine/threonine-protein kinase RIP
, receptor (TNFRSF)-interacting serine-threonine kinase 1
, receptor interacting serine/threonine kinase 1 L homeolog
, receptor-interacting protein 1 beta